Magnesium in PDB 1aq2: Phosphoenolpyruvate Carboxykinase

All present enzymatic activity of Phosphoenolpyruvate Carboxykinase:
4.1.1.49;

The structure of Phosphoenolpyruvate Carboxykinase, PDB code: 1aq2 was solved by L.W.Tari, A.Matte, H.Goldie, L.T.J.Delbaere, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	6.00 / 1.90
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	126.190, 96.610, 46.860, 90.00, 95.80, 90.00
R / Rfree (%)	21.8 / 26

The structure of Phosphoenolpyruvate Carboxykinase also contains other interesting chemical elements:

Manganese

(Mn)

1 atom

The binding sites of Magnesium atom in the Phosphoenolpyruvate Carboxykinase (pdb code 1aq2). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Phosphoenolpyruvate Carboxykinase, PDB code: 1aq2:

Magnesium binding site 1 out of 1 in the Phosphoenolpyruvate Carboxykinase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Phosphoenolpyruvate Carboxykinase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg544 b:20.8 occ:1.00 O2B A:ATP541 2.1 26.5 1.0 O3G A:ATP541 2.1 28.9 1.0 O A:HOH546 2.2 16.8 1.0 OG1 A:THR255 2.2 21.6 1.0 O A:HOH747 2.2 18.8 1.0 O A:HOH746 2.2 23.7 1.0 CB A:THR255 3.2 26.6 1.0 PB A:ATP541 3.4 21.4 1.0 PG A:ATP541 3.4 20.4 1.0 OD2 A:ASP268 3.7 21.1 1.0 O A:TYR286 3.7 19.4 1.0 O3B A:ATP541 3.8 20.6 1.0 O2A A:ATP541 3.9 22.9 1.0 O1G A:ATP541 4.1 16.3 1.0 N A:THR255 4.1 24.5 1.0 OD1 A:ASP269 4.2 18.6 1.0 CA A:THR255 4.2 21.5 1.0 O A:ASP268 4.2 21.2 1.0 CG2 A:THR255 4.2 14.7 1.0 NH1 A:ARG333 4.3 26.4 1.0 O3A A:ATP541 4.3 18.0 1.0 PA A:ATP541 4.4 22.4 1.0 O A:HOH547 4.5 23.9 1.0 O2G A:ATP541 4.5 24.0 1.0 CG A:ASP268 4.5 24.7 1.0 O1B A:ATP541 4.5 23.1 1.0 O1A A:ATP541 4.5 28.1 1.0 C A:TYR286 4.7 19.6 1.0 CG A:ASP269 4.9 23.2 1.0 O A:HOH604 4.9 21.6 1.0 CB A:ASP269 5.0 21.0 1.0

L.W.Tari, A.Matte, H.Goldie, L.T.Delbaere. Mg(2+)-MN2+ Clusters in Enzyme-Catalyzed Phosphoryl-Transfer Reactions. Nat.Struct.Biol. V. 4 990 1997.
ISSN: ISSN 1072-8368
PubMed: 9406547
DOI: 10.1038/NSB1297-990